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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1993-6-10
|
| pubmed:abstractText |
Human hepatoma Li-7A cells exhibit two cell surface ATPase (ectoATPase) activities distinguishable by their different biochemical properties. The activity of the minor ectoATPase, ectoCa(2+)-ATPase, is enhanced severalfold when Li-7A cells are treated simultaneously by epidermal growth factor (EGF) and cAMP elevating agents (Knowles, A. F., 1990, Arch. Biochem. Biophys. 283, 114-119). Here we report that the human ectoCa(2+)-ATPase is biochemically similar to the major rat hepatocyte ectoATPase/cell adhesion molecule (cell-CAM 105) with respect to response to divalent ions and sulfhydryl reagents. Furthermore, the binding of rat liver ectoATPase antibody increased markedly in EGF/cholera toxin/hydrocortisone-treated Li-7A cells compared to untreated cells. Western blot analysis revealed cross-reactivity of the antibody with a 125-kDa protein. Partial purification of ectoCa(2+)-ATPase from EGF/cholera toxin/hydrocortisone-treated Li-7A cells confirmed that enrichment of the 125-kDa protein correlated with an increase in ATPase activity. We conclude that EGF and increased levels of cAMP lead to increased synthesis of the ectoCa(2+)-ATPase in Li-7A cells. The present demonstration of similarity between the ectoCa(2+)-ATPase and a rat liver cell adhesion molecule, cell-CAM 105, contributes significantly to an understanding of the implication of down-regulation of ectoCa(2+)-ATPase during hepatocyte-hepatoma transformation.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Cholera Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrocortisone,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/ectoATPase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0003-9861
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
303
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
90-7
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:8387753-Adenosine Triphosphatases,
pubmed-meshheading:8387753-Animals,
pubmed-meshheading:8387753-Blotting, Western,
pubmed-meshheading:8387753-Calcium,
pubmed-meshheading:8387753-Calcium-Transporting ATPases,
pubmed-meshheading:8387753-Carcinoma, Hepatocellular,
pubmed-meshheading:8387753-Cell Membrane,
pubmed-meshheading:8387753-Cholera Toxin,
pubmed-meshheading:8387753-Cross Reactions,
pubmed-meshheading:8387753-Cyclic AMP,
pubmed-meshheading:8387753-Enzyme Induction,
pubmed-meshheading:8387753-Epidermal Growth Factor,
pubmed-meshheading:8387753-Extracellular Space,
pubmed-meshheading:8387753-Humans,
pubmed-meshheading:8387753-Hydrocortisone,
pubmed-meshheading:8387753-Liver,
pubmed-meshheading:8387753-Liver Neoplasms,
pubmed-meshheading:8387753-Magnesium,
pubmed-meshheading:8387753-Molecular Weight,
pubmed-meshheading:8387753-Rats,
pubmed-meshheading:8387753-Tumor Cells, Cultured
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
The epidermal growth factor/cAMP-inducible ectoCa(2+)-ATPase of human hepatoma Li-7A cells is similar to rat liver ectoATPase/hepatocyte cell adhesion molecule (cell-CAM 105).
|
| pubmed:affiliation |
Department of Biology, Northeastern University, Boston, Massachusetts 02115.
|
| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
|